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Background The aim of this work was to purify and characterize the exo-β-1,3-glucanase, namely Tt BgnA, from the thermophilic fungus Thielavia terrestris Co3Bag1; and to identify the purified enzyme. Results The thermophile biomass-degrading fungus T. terrestris Co3Bag1 displayed β-1,3-glucanase activity when grown on 1% glucose. An exo-β-1,3-glucanase, with an estimated molecular mass of 129 kDa, named Tt BgnA, was purified from culture filtrates from T. terrestris Co3Bag1. The enzyme exhibited optimum activity at pH 6.0 and 70°C, and half-lives ( t ½ ) of 54, and 37 min at 50 and 60°C, respectively. Substrate specificity analysis showed that laminarin was the best substrate studied for Tt BgnA. When laminarin was used as the substrate, the apparent K M and V max values were determined to be 2.2 mg mL −1 and 10.8 U/mg, respectively. Analysis of hydrolysis products by thin-layer chromatography (TLC) revealed Tt BgnA displays an exo mode of action. Additionally, the enzyme was partially sequenced by tandem mass spectrometry (MS/MS), and the results suggested that Tt BgnA from T. terrestris Co3Bag1 could be classified as a member of the GH-31 family. Conclusions This report thus describes the purification and characterization of Tt BgnA, a novel exo-β-1,3-glucanase GH-31 family from the thermophilic fungus T. terrestris Co3Bag1. Based on the biochemical properties displayed by Tt BgnA, the enzyme could be considered as a candidate for potential biotechnological applications.

electronic journal of biotechnology

Purification and biochemical characterization of a novel thermophilic exo-β-1,3-glucanase from the thermophile biomass-degrading fungus Thielavia terrestris Co3Bag1